Zobrazeno 1 - 10
of 119
pro vyhledávání: '"James L Cole"'
Autor:
Christopher Wostenberg, Jeffrey W Lary, Debashish Sahu, Roderico Acevedo, Kaycee A Quarles, James L Cole, Scott A Showalter
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e51829 (2012)
One of the most exciting recent developments in RNA biology has been the discovery of small non-coding RNAs that affect gene expression through the RNA interference (RNAi) mechanism. Two major classes of RNAs involved in RNAi are small interfering RN
Externí odkaz:
https://doaj.org/article/a495af3b5fc34f73aa52fe242ced41ff
Publikováno v:
ACS Omega, Vol 6, Iss 17, Pp 11367-11374 (2021)
Externí odkaz:
https://doaj.org/article/78d2437043704164a7c23455bc5440fc
Autor:
Christopher B. Mayo, James L. Cole
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
Abstract Although the antiviral kinase PKR was originally characterized as a double-stranded RNA activated enzyme it can be stimulated by RNAs containing limited secondary structure. Single-stranded regions in such RNAs contribute to binding and acti
Externí odkaz:
https://doaj.org/article/9e6d55f8d40d4cf4ba648d3cf513a13b
Publikováno v:
FEBS Letters. 596:479-490
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6de553e97ecef781d143cd196cd3d130
https://doi.org/10.1002/1873-3468.14276
https://doi.org/10.1002/1873-3468.14276
Publikováno v:
ACS Omega
ACS Omega, Vol 6, Iss 17, Pp 11367-11374 (2021)
ACS Omega, Vol 6, Iss 17, Pp 11367-11374 (2021)
Protein kinase R (PKR) is a key pattern recognition receptor of the innate immune pathway. PKR is activated by double-stranded RNA (dsRNA) that is often produced during viral genome replication and transcription. PKR contains two tandem double-strand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b61cbd35b87f736ef74396f170075ce
http://europepmc.org/articles/PMC8153938
http://europepmc.org/articles/PMC8153938
Autor:
Cassie M. Zerbe, James L. Cole
Publikováno v:
Biochemistry. 59:1252-1260
Protein kinase R (PKR) is a key antiviral component of the innate immune pathway and is activated by viral double-stranded RNAs (dsRNAs). Adenovirus-associated RNA 1 (VAI) is an abundant, noncoding viral RNA that functions as a decoy by binding PKR b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad6814ff60ecf902b0d78db310574db9
https://doi.org/10.1021/acs.biochem.0c00088
https://doi.org/10.1021/acs.biochem.0c00088
Autor:
Thomas E. Sladewski, Paul C. Campbell, Neil Billington, Alexandra D’Ordine, James L. Cole, Christopher L. de Graffenried
Publikováno v:
Current Biology. 33:899-911.e5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::322e39b453cacccf473aacd386f7d18e
https://doi.org/10.1016/j.cub.2023.01.035
https://doi.org/10.1016/j.cub.2023.01.035
Publikováno v:
Protein Sci
The innate immune system is the first line of defense against invading pathogens. The retinoic acid‐inducible gene I (RIG‐I) like receptors (RLRs), RIG‐I and melanoma differentiation‐associated protein 5 (MDA5), are critical for host recognit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa37746a9b2800723c18c5a35a54731d
https://doi.org/10.1002/pro.3776
https://doi.org/10.1002/pro.3776
Autor:
Christopher B. Mayo, Heidi Erlandsen, David J. Mouser, Aaron G. Feinstein, Victoria L. Robinson, Eric R. May, James L. Cole
Publikováno v:
Biochemistry
The RNA-activated protein kinase, PKR, is a key mediator of the innate immunity response to viral infection. Viral double-stranded RNAs induce PKR dimerization and autophosphorylation. The PKR kinase domain forms a back-to-back dimer. However, interm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d824e4f9e4c9c3adb768e316e5d9a09
https://doi.org/10.1021/acs.biochem.9b00161
https://doi.org/10.1021/acs.biochem.9b00161
Autor:
Deepthi L Anipindi, Heidi Erlandsen, James L. Cole, Brian J. Maniaci, Tom Huxford, John J. Love, Colin H. Lipper, Boguslaw Stec
Publikováno v:
Biochemistry. 58:2199-2207
The ability to precisely control protein complex formation has high utility in the expanding field of biomaterials. Driving protein-protein binding through metal-ligand bridging interactions is a promising method of achieving this goal. Furthermore,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9f2ad6091f262c143e9f9849454ffe7
https://doi.org/10.1021/acs.biochem.9b00055
https://doi.org/10.1021/acs.biochem.9b00055